ID A0A248JLU6_9PROT Unreviewed; 822 AA.
AC A0A248JLU6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:ASG19516.1};
GN ORFNames=Y958_00775 {ECO:0000313|EMBL:ASG19516.1};
OS Nitrospirillum viridazoti CBAmc.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodospirillales; Azospirillaceae; Nitrospirillum;
OC Nitrospirillum viridazoti.
OX NCBI_TaxID=1441467 {ECO:0000313|EMBL:ASG19516.1, ECO:0000313|Proteomes:UP000197153};
RN [1] {ECO:0000313|EMBL:ASG19516.1, ECO:0000313|Proteomes:UP000197153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBAmC {ECO:0000313|EMBL:ASG19516.1,
RC ECO:0000313|Proteomes:UP000197153};
RA Schwab S., dos Santos Teixeira K.R., Simoes Araujo J.L., Soares Vidal M.,
RA Borges de Freitas H.R., Rivello Crivelaro A.L., Bueno de Camargo Nunes A.,
RA dos Santos C.M., Palmeira da Silva Rosa D., da Silva Padilha D.,
RA da Silva E., Araujo Terra L., Soares Mendes V., Farinelli L.,
RA Magalhaes Cruz L., Baldani J.I.;
RT "Complete genome sequence of Nitrospirillum amazonense strain CBAmC, an
RT endophytic nitrogen-fixing and plant growth-promoting bacterium, isolated
RT from sugarcane.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR EMBL; CP022110; ASG19516.1; -; Genomic_DNA.
DR RefSeq; WP_088870516.1; NZ_CP022110.1.
DR AlphaFoldDB; A0A248JLU6; -.
DR KEGG; nao:Y958_00775; -.
DR Proteomes; UP000197153; Chromosome 1.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd14752; GH31_N; 1.
DR CDD; cd06591; GH31_xylosidase_XylS; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR InterPro; IPR033403; DUF5110.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR017853; GH.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR051816; Glycosyl_Hydrolase_31.
DR PANTHER; PTHR43863; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G03140)-RELATED; 1.
DR PANTHER; PTHR43863:SF2; MALTASE-GLUCOAMYLASE; 1.
DR Pfam; PF17137; DUF5110; 1.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|RuleBase:RU361185};
KW Reference proteome {ECO:0000313|Proteomes:UP000197153};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..41
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 42..822
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013032531"
FT DOMAIN 158..265
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 307..646
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 654..741
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 759..802
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
SQ SEQUENCE 822 AA; 91371 MW; D5533B3A15635968 CRC64;
MKTQGQPARG ATPKSMLNYR GLALVLGLGA AASALTTPAL AADRDVTAAM VVDQSNKTQE
QTLVLEPYGP NIIRVTLSLK KDAALAGPGY GIIPGANPAG WTQGQDERGD TVLKSGQMSA
TIVGWHPPPH AVPPQQTAVD ISRYFGGTTN GAHILFKDAA GKTILDFTGW SMGIPNFKDG
NSQLLHDRRP TDDQFYTVNG TFASPADEHY YGLGQNQEGF LDHRGHVVRC WNDYNASGGQ
STCVPFMITN YGYGLLWDNP SKTTIEPGFN EVTRWTSEVG DRVSFFVISG KTPDEIYAGY
RQLTGATPML PKSAYGYIQS KQRYRSQQEV LDVAKGYRER HIPADVLVVD WFYYTIMGQF
DFVPELWPNP KAMNKQLHDM GFETMISVWP RFTSDGRYYD LLKKNGWFLS QADGTPTNGL
PYDKAGSDID TTNPDAAKWY WNTIRDNILS QGFDSLWSDE TEPDLPPNGS YYHIGPGTKY
FNVYPLFHTS ALYDGFRRDF KDKRTVILSR DAYLGVQRNG AIVWSSDITP TWDAFKRQVP
TGLDFAASGI TYWSNDTGGW QYLPEEHKPA KAPLLDPTPA RGVVGGYDDY PELYTRWFQY
ATFLPVLRTH GSRPANEIWS YGPDAQAILE KYVKLRYQLI PYIYSLGYKT YKTGAPFLRA
LPLDFPNDPA VTDMRDEYMF GPALLVAPVT EQGATTKQVY LPAGSDWYDF WTDKRYTGGQ
TVTVAAPIDR IPVFVKAGSI LPLGSPIENT HQKQTIAKVK VYPGADGRFT LFQDDGFTYA
YEQGGGNVTE LSWSEASHSL GHTGAKGWSE PDAKVVEVVQ AK
//
